SETB1_DROME
ID SETB1_DROME Reviewed; 1262 AA.
AC Q32KD2; Q29QW7; Q8IHC9; Q8MMD1; Q960X1; Q9W110;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Histone-lysine N-methyltransferase eggless;
DE EC=2.1.1.355;
DE AltName: Full=SETDB1 homolog;
GN Name=egg; ORFNames=CG12196;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley;
RA Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M.,
RA Park S., Wan K.H., Yu C., Celniker S.E.;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 378-1262.
RC STRAIN=Berkeley; TISSUE=Embryo, and Testis;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP AND DISRUPTION PHENOTYPE.
RX PubMed=17164421; DOI=10.1242/dev.02698;
RA Clough E., Moon W., Wang S., Smith K., Hazelrigg T.;
RT "Histone methylation is required for oogenesis in Drosophila.";
RL Development 134:157-165(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-215 AND THR-217, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
CC -!- FUNCTION: Histone methyltransferase that specifically trimethylates
CC 'Lys-9' of histone H3 in ovary. H3 'Lys-9' trimethylation represents a
CC specific tag for epigenetic transcriptional repression by recruiting
CC Su(var)205/HP1 to methylated histones. Plays a central role during
CC oogenesis. {ECO:0000269|PubMed:17164421}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysyl(9)-[histone H3] + 3 S-adenosyl-L-methionine = 3 H(+) +
CC N(6),N(6),N(6)-trimethyl-L-lysyl(9)-[histone H3] + 3 S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:60276, Rhea:RHEA-COMP:15538, Rhea:RHEA-
CC COMP:15546, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61961; EC=2.1.1.355;
CC -!- INTERACTION:
CC Q32KD2; Q9W123: Pof; NbExp=2; IntAct=EBI-140830, EBI-155974;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17164421}. Chromosome
CC {ECO:0000305|PubMed:17164421}.
CC -!- TISSUE SPECIFICITY: Expressed in ovary (at protein level).
CC {ECO:0000269|PubMed:17164421}.
CC -!- DEVELOPMENTAL STAGE: Present most strongly at early stages of
CC oogenesis, in germ cells in the germarium. Present in germ stem cells
CC and dividing germline cyst cells. Weakly or not expressed in somatic
CC cells at the tip of the germarium, including the terminal filament,
CC inner sheath cells, or cap cells, but it is present at low levels in
CC somatic cells in regions 2 and 3 of the germarium, including the
CC prefollicular cells and the follicle cells of stage 1 egg chambers.
CC Soon after egg chambers budd off the germarium, levels increase in the
CC follicle cells. By mid-oogenesis it decreases in the nurse cells, while
CC levels continued to increase in the follicle cells (at protein level).
CC {ECO:0000269|PubMed:17164421}.
CC -!- DOMAIN: In the pre-SET domain, Cys residues bind 3 zinc ions that are
CC arranged in a triangular cluster; some of these Cys residues contribute
CC to the binding of two zinc ions within the cluster. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Oogenesis arrests at early stages. This arrest is
CC accompanied by reduced proliferation of somatic cells required for egg
CC chamber formation, and by apoptosis in both germ and somatic cell
CC populations. {ECO:0000269|PubMed:17164421}.
CC -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase
CC superfamily. Histone-lysine methyltransferase family. Suvar3-9
CC subfamily. {ECO:0000255|PROSITE-ProRule:PRU00190}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK93223.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAN71064.2; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=ABC86335.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE013599; AAF47268.3; -; Genomic_DNA.
DR EMBL; BT023947; ABB36451.1; -; mRNA.
DR EMBL; BT024273; ABC86335.1; ALT_INIT; mRNA.
DR EMBL; AY051799; AAK93223.1; ALT_INIT; mRNA.
DR EMBL; BT001309; AAN71064.2; ALT_INIT; mRNA.
DR RefSeq; NP_611966.3; NM_138122.5.
DR AlphaFoldDB; Q32KD2; -.
DR SMR; Q32KD2; -.
DR BioGRID; 63532; 34.
DR DIP; DIP-46503N; -.
DR IntAct; Q32KD2; 8.
DR STRING; 7227.FBpp0111689; -.
DR iPTMnet; Q32KD2; -.
DR PaxDb; Q32KD2; -.
DR PRIDE; Q32KD2; -.
DR DNASU; 37962; -.
DR EnsemblMetazoa; FBtr0112777; FBpp0111689; FBgn0086908.
DR GeneID; 37962; -.
DR KEGG; dme:Dmel_CG12196; -.
DR CTD; 37962; -.
DR FlyBase; FBgn0086908; egg.
DR VEuPathDB; VectorBase:FBgn0086908; -.
DR eggNOG; KOG1141; Eukaryota.
DR GeneTree; ENSGT00940000169356; -.
DR HOGENOM; CLU_003279_0_1_1; -.
DR InParanoid; Q32KD2; -.
DR OMA; YCQCGAP; -.
DR OrthoDB; 183716at2759; -.
DR PhylomeDB; Q32KD2; -.
DR BRENDA; 2.1.1.355; 1994.
DR Reactome; R-DME-3214841; PKMTs methylate histone lysines.
DR SignaLink; Q32KD2; -.
DR BioGRID-ORCS; 37962; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 37962; -.
DR PRO; PR:Q32KD2; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0086908; Expressed in eye disc (Drosophila) and 47 other tissues.
DR Genevisible; Q32KD2; DM.
DR GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005700; C:polytene chromosome; IDA:FlyBase.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0046974; F:histone methyltransferase activity (H3-K9 specific); IDA:FlyBase.
DR GO; GO:0018024; F:histone-lysine N-methyltransferase activity; IMP:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0048132; P:female germ-line stem cell asymmetric division; IDA:FlyBase.
DR GO; GO:0080188; P:gene silencing by RNA-directed DNA methylation; IMP:FlyBase.
DR GO; GO:0031507; P:heterochromatin assembly; IMP:FlyBase.
DR GO; GO:0070828; P:heterochromatin organization; IMP:FlyBase.
DR GO; GO:0051567; P:histone H3-K9 methylation; IDA:FlyBase.
DR GO; GO:0010629; P:negative regulation of gene expression; IGI:FlyBase.
DR GO; GO:0051038; P:negative regulation of transcription involved in meiotic cell cycle; IMP:UniProtKB.
DR GO; GO:0048477; P:oogenesis; IDA:FlyBase.
DR GO; GO:0090309; P:positive regulation of DNA methylation-dependent heterochromatin assembly; IMP:FlyBase.
DR GO; GO:0040029; P:regulation of gene expression, epigenetic; IMP:FlyBase.
DR Gene3D; 2.170.270.10; -; 1.
DR InterPro; IPR016177; DNA-bd_dom_sf.
DR InterPro; IPR001739; Methyl_CpG_DNA-bd.
DR InterPro; IPR003616; Post-SET_dom.
DR InterPro; IPR007728; Pre-SET_dom.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR InterPro; IPR041292; Tudor_4.
DR InterPro; IPR041291; TUDOR_5.
DR Pfam; PF01429; MBD; 1.
DR Pfam; PF05033; Pre-SET; 1.
DR Pfam; PF00856; SET; 1.
DR Pfam; PF18358; Tudor_4; 1.
DR Pfam; PF18359; Tudor_5; 1.
DR SMART; SM00391; MBD; 1.
DR SMART; SM00468; PreSET; 1.
DR SMART; SM00317; SET; 1.
DR SUPFAM; SSF54171; SSF54171; 1.
DR SUPFAM; SSF82199; SSF82199; 1.
DR PROSITE; PS50982; MBD; 1.
DR PROSITE; PS50868; POST_SET; 1.
DR PROSITE; PS50867; PRE_SET; 1.
DR PROSITE; PS50280; SET; 1.
PE 1: Evidence at protein level;
KW Chromatin regulator; Chromosome; Coiled coil; Developmental protein;
KW Differentiation; Metal-binding; Methyltransferase; Nucleus; Oogenesis;
KW Phosphoprotein; Reference proteome; Repeat; Repressor;
KW S-adenosyl-L-methionine; Transcription; Transcription regulation;
KW Transferase; Zinc.
FT CHAIN 1..1262
FT /note="Histone-lysine N-methyltransferase eggless"
FT /id="PRO_0000281822"
FT DOMAIN 529..602
FT /note="Tudor 1"
FT DOMAIN 629..686
FT /note="Tudor 2"
FT DOMAIN 818..884
FT /note="MBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00338"
FT DOMAIN 946..1018
FT /note="Pre-SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00157"
FT DOMAIN 1021..1237
FT /note="SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT DOMAIN 1246..1262
FT /note="Post-SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00155"
FT REGION 1..194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 743..764
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1086..1148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 353..420
FT /evidence="ECO:0000255"
FT COMPBIAS 1..22
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 84..100
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 132..152
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 166..183
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1093..1109
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1127..1148
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 948
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 948
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 950
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 954
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 954
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 960
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 962
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 1000
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 1000
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 1004
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 1006
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 1010
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 1031..1033
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 1069
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT BINDING 1071
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT BINDING 1191
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT BINDING 1194..1195
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 1197
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 1250
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 1252
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 1257
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT MOD_RES 215
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 217
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
SQ SEQUENCE 1262 AA; 141946 MW; A89DFF1CC6FCED1C CRC64;
MSGQPTAVDC LESSGSTVED VQETPASREK SYGLPVRKGE NSLESPAEQA AKDVEIEELT
HSEAIAATGS TRKQCPYGGK APDEPGKLAD ESEDRKGENT KAIASSPVLV AVDSDSSVEL
IESPVKFSSA NESEKDPPKP DAVNEAAAKE AEEMTDSSIS SPTSESFPEK DEKTNKENEQ
EPPGMEVDQD VEESISRPAE EYKIENTLKG HKRISLTEIE EHKIVDKKDD VLEVELEKGT
APKAAEDEKL NALLSDGDVF YDKECVNCNC TKLHKQYVLA NMATLNFYQV LRKSSKQQFL
CMGCHDTAMD LYEEYAGQLM AKQPLLLKDF HQDHADFVAL DSSDEEEEEK QPEKSDFSKN
KLQLIEDELD DAIKNVLNKV DFTAQLSWSK TILQAKADHL ERQFALADVE LEKVQTTADK
MHCALYNSCP VAHKHLPTLD IEPSDYVHEV PPPGEIVRPP IQLGETYYAV KNKAIASWVS
IKVIEFTEST AINGNTMKSY KIRYLNTPYQ MIKTVTAKHI AYFEPPPVRL TIGTRVIAYF
DGTTLSRGKD KGVVQSAFYP GIIAEPLKQA NRYRYLIFYD DGYTQYVPHR DVRLVCQASE
KVWEDVHAAS RDFIQKYVEK YSVDRPMVQC TRGQSMTTES NGTWLYARVI DIDCSLVLMQ
FEGDKNHTEW IYRGSLRLGP VFRETQNNMN SSSAQQLRVP RRTEPFIRYT KEMESSSKVN
QQMRAFARKS SASAQNNALA AASSAATPAG GRTNAGGVST SNSASAVRHL NNSTIYVDDE
NRPKGHVVYF TAKRNLPPKM YKCHECSPNC LFKIVHRLDS YSPLAKPLLS GWERLVMRQK
TKKSVVYKGP CGKSLRSLAE VHRYLRATEN VLNVDNFDFT PDLKCLAEYS IDPSIVKDTD
ISKGQEKMAI PLVNYYDNTL PPPCTYAKQR IPTEGVHLNL DEEFLLCCDC EDDCSDKSKC
ACWQLTVAGV RYCNPKKPIE EIGYQYKRLH EHVPTGIYEC NSRCKCKKNC LNRVVQFSLE
MKLQVFKTSN RGWGLRCVND IPKGAFICIY AGHLLTETMA NEGGQDAGDE YFADLDYIEV
AEQLKEGYES EVDHSDPDAE EDNGGPDAED DDDFRPNYHY QRKIKRSSRS GSTQNSSTQS
SELDSQERAV INFNPNADLD ETVRENSVRR LFGKDEAPYI MDAKTTGNLG RYFNHSCSPN
LFVQNVFVDT HDLRFPWVAF FSAAHIRSGT ELTWNYNYEV GVVPGKVLYC QCGAPNCRLR
LL
